Biology:GHKL domain

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Short description: Evolutionary conserved protein domain
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
PDB 1ah6 EBI.jpg
Structure of the N-terminal domain of the yeast Hsp90 chaperone.[1]
Identifiers
SymbolHATPase_c
PfamPF02518
InterProIPR003594
SMARTHATPase_c
SCOP21ei1 / SCOPe / SUPFAM
CDDcd00075

The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain.[2] It is an ATPase domain found in several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases,[3] heat shock protein HSP90,[4][5][6] phytochrome-like ATPases and DNA mismatch repair proteins.

More information about this protein can be found at Protein of the Month: DNA Topoisomerase.[7]

Structure

The fold of this domain consists of two layers, alpha/beta, which contain an 8-stranded mixed beta-sheet.[2]

Subfamilies

  • Heat shock protein Hsp90, N-terminal

InterProIPR020575

  • Sensor histidine kinase NatK, C-terminal domain

InterProIPR032834

Members

References

  1. "A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone". Nat. Struct. Biol. 4 (6): 477–82. June 1997. doi:10.1038/nsb0697-477. PMID 9187656. 
  2. 2.0 2.1 "GHKL, an emergent ATPase/kinase superfamily". Trends Biochem. Sci. 25 (1): 24–8. January 2000. doi:10.1016/S0968-0004(99)01503-0. PMID 10637609. 
  3. "Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase". Antimicrob. Agents Chemother. 48 (5): 1856–64. May 2004. doi:10.1128/AAC.48.5.1856-1864.2004. PMID 15105144. 
  4. "Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone". J. Biol. Chem. 279 (44): 46162–71. October 2004. doi:10.1074/jbc.M405253200. PMID 15292259. 
  5. "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell 116 (1): 87–98. January 2004. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169. 
  6. "Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms". Chem. Biol. 11 (6): 775–85. June 2004. doi:10.1016/j.chembiol.2004.03.033. PMID 15217611. 
  7. McDowall J (2006). "DNA Topoisomerase". Protein of the month. InterPro. http://www.ebi.ac.uk/interpro/potm/2006_1/Page1.htm. 
This article incorporates text from the public domain Pfam and InterPro: IPR003594